Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
ABSTRACT: Background: RNA post-transcriptional modification is an exciting field of research that has evidenced this editing process as a sophisticated epigenetic mechanism to fine tune the ribosome function and to control gene expression. Although tRNA modifications seem to be more relevant for the...
- Autores:
-
Mosquera Rendón, Jeanneth
Cárdenas Brito, Sonia
Pineda Cárdenas, Juan David
Corredor Rodríguez, Mauricio
Benítez Páez, Alfonso
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2014
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/22179
- Acceso en línea:
- http://hdl.handle.net/10495/22179
- Palabra clave:
- Evolución Molecular
Evolution, Molecular
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Bacteria
Bacterias
RNA methyltransferases
Conserved sequence motifs
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by/2.5/co/
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|
dc.title.spa.fl_str_mv |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases |
title |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases |
spellingShingle |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases Evolución Molecular Evolution, Molecular Farmacorresistencia Microbiana Drug Resistance, Microbial Bacteria Bacterias RNA methyltransferases Conserved sequence motifs |
title_short |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases |
title_full |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases |
title_fullStr |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases |
title_full_unstemmed |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases |
title_sort |
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases |
dc.creator.fl_str_mv |
Mosquera Rendón, Jeanneth Cárdenas Brito, Sonia Pineda Cárdenas, Juan David Corredor Rodríguez, Mauricio Benítez Páez, Alfonso |
dc.contributor.author.none.fl_str_mv |
Mosquera Rendón, Jeanneth Cárdenas Brito, Sonia Pineda Cárdenas, Juan David Corredor Rodríguez, Mauricio Benítez Páez, Alfonso |
dc.subject.decs.none.fl_str_mv |
Evolución Molecular Evolution, Molecular Farmacorresistencia Microbiana Drug Resistance, Microbial Bacteria Bacterias |
topic |
Evolución Molecular Evolution, Molecular Farmacorresistencia Microbiana Drug Resistance, Microbial Bacteria Bacterias RNA methyltransferases Conserved sequence motifs |
dc.subject.proposal.spa.fl_str_mv |
RNA methyltransferases Conserved sequence motifs |
description |
ABSTRACT: Background: RNA post-transcriptional modification is an exciting field of research that has evidenced this editing process as a sophisticated epigenetic mechanism to fine tune the ribosome function and to control gene expression. Although tRNA modifications seem to be more relevant for the ribosome function and cell physiology as a whole, some rRNA modifications have also been seen to play pivotal roles, essentially those located in central ribosome regions. RNA methylation at nucleobases and ribose moieties of nucleotides appear to frequently modulate its chemistry and structure. RNA methyltransferases comprise a superfamily of highly specialized enzymes that accomplish a wide variety of modifications. These enzymes exhibit a poor degree of sequence similarity in spite of using a common reaction cofactor and modifying the same substrate type. Results: Relationships and lineages of RNA methyltransferases have been extensively discussed, but no consensus has been reached. To shed light on this topic, we performed amino acid and codon-based sequence analyses to determine phylogenetic relationships and molecular evolution. We found that most Class I RNA MTases are evolutionarily related to protein and cofactor/vitamin biosynthesis methyltransferases. Additionally, we found that at least nine lineages explain the diversity of RNA MTases. We evidenced that RNA methyltransferases have high content of polar and positively charged amino acid, which coincides with the electrochemistry of their substrates. Conclusions: After studying almost 12,000 bacterial genomes and 2,000 patho-pangenomes, we revealed that molecular evolution of Class I methyltransferases matches the different rates of synonymous and non-synonymous substitutions along the coding region. Consequently, evolution on Class I methyltransferases selects against amino acid changes affecting the structure conformation |
publishDate |
2014 |
dc.date.issued.none.fl_str_mv |
2014 |
dc.date.accessioned.none.fl_str_mv |
2021-09-04T01:54:35Z |
dc.date.available.none.fl_str_mv |
2021-09-04T01:54:35Z |
dc.type.spa.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.hasversion.spa.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.coar.spa.fl_str_mv |
http://purl.org/coar/resource_type/c_2df8fbb1 |
dc.type.redcol.spa.fl_str_mv |
https://purl.org/redcol/resource_type/ART |
dc.type.local.spa.fl_str_mv |
Artículo de investigación |
format |
http://purl.org/coar/resource_type/c_2df8fbb1 |
status_str |
publishedVersion |
dc.identifier.citation.spa.fl_str_mv |
Mosquera, J., Cárdenas, S., Pineda, J., Corredor, M., & Benítez, A. (2014) Relaciones evolutivas y basadas en secuencias en metiltransferasas de ARN no codificantes dependientes de AdoMet bacterianas. BMC Res Notes 7, 440. https://doi.org/10.1186/1756-0500-7-440 |
dc.identifier.uri.none.fl_str_mv |
http://hdl.handle.net/10495/22179 |
dc.identifier.doi.none.fl_str_mv |
10.1186/1756-0500-7-440 |
dc.identifier.eissn.none.fl_str_mv |
1756-0500 |
identifier_str_mv |
Mosquera, J., Cárdenas, S., Pineda, J., Corredor, M., & Benítez, A. (2014) Relaciones evolutivas y basadas en secuencias en metiltransferasas de ARN no codificantes dependientes de AdoMet bacterianas. BMC Res Notes 7, 440. https://doi.org/10.1186/1756-0500-7-440 10.1186/1756-0500-7-440 1756-0500 |
url |
http://hdl.handle.net/10495/22179 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofjournalabbrev.spa.fl_str_mv |
BMC Res. Notes. |
dc.rights.spa.fl_str_mv |
info:eu-repo/semantics/openAccess |
dc.rights.uri.*.fl_str_mv |
http://creativecommons.org/licenses/by/2.5/co/ |
dc.rights.accessrights.spa.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.creativecommons.spa.fl_str_mv |
https://creativecommons.org/licenses/by-nc-nd/4.0/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/2.5/co/ http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by-nc-nd/4.0/ |
dc.format.extent.spa.fl_str_mv |
15 |
dc.format.mimetype.spa.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
BMC |
dc.publisher.group.spa.fl_str_mv |
GEBIOMIC (Genética y Bioquímica de Microorganismos) |
dc.publisher.place.spa.fl_str_mv |
Londres, Inglaterra |
institution |
Universidad de Antioquia |
bitstream.url.fl_str_mv |
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bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositorio Institucional Universidad de Antioquia |
repository.mail.fl_str_mv |
andres.perez@udea.edu.co |
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1812173223980171264 |
spelling |
Mosquera Rendón, JeannethCárdenas Brito, SoniaPineda Cárdenas, Juan DavidCorredor Rodríguez, MauricioBenítez Páez, Alfonso2021-09-04T01:54:35Z2021-09-04T01:54:35Z2014Mosquera, J., Cárdenas, S., Pineda, J., Corredor, M., & Benítez, A. (2014) Relaciones evolutivas y basadas en secuencias en metiltransferasas de ARN no codificantes dependientes de AdoMet bacterianas. BMC Res Notes 7, 440. https://doi.org/10.1186/1756-0500-7-440http://hdl.handle.net/10495/2217910.1186/1756-0500-7-4401756-0500ABSTRACT: Background: RNA post-transcriptional modification is an exciting field of research that has evidenced this editing process as a sophisticated epigenetic mechanism to fine tune the ribosome function and to control gene expression. Although tRNA modifications seem to be more relevant for the ribosome function and cell physiology as a whole, some rRNA modifications have also been seen to play pivotal roles, essentially those located in central ribosome regions. RNA methylation at nucleobases and ribose moieties of nucleotides appear to frequently modulate its chemistry and structure. RNA methyltransferases comprise a superfamily of highly specialized enzymes that accomplish a wide variety of modifications. These enzymes exhibit a poor degree of sequence similarity in spite of using a common reaction cofactor and modifying the same substrate type. Results: Relationships and lineages of RNA methyltransferases have been extensively discussed, but no consensus has been reached. To shed light on this topic, we performed amino acid and codon-based sequence analyses to determine phylogenetic relationships and molecular evolution. We found that most Class I RNA MTases are evolutionarily related to protein and cofactor/vitamin biosynthesis methyltransferases. Additionally, we found that at least nine lineages explain the diversity of RNA MTases. We evidenced that RNA methyltransferases have high content of polar and positively charged amino acid, which coincides with the electrochemistry of their substrates. Conclusions: After studying almost 12,000 bacterial genomes and 2,000 patho-pangenomes, we revealed that molecular evolution of Class I methyltransferases matches the different rates of synonymous and non-synonymous substitutions along the coding region. Consequently, evolution on Class I methyltransferases selects against amino acid changes affecting the structure conformationCOL001406415application/pdfengBMCGEBIOMIC (Genética y Bioquímica de Microorganismos)Londres, Inglaterrainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARTArtículo de investigaciónhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/co/http://purl.org/coar/access_right/c_abf2https://creativecommons.org/licenses/by-nc-nd/4.0/Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferasesEvolución MolecularEvolution, MolecularFarmacorresistencia MicrobianaDrug Resistance, MicrobialBacteriaBacteriasRNA methyltransferasesConserved sequence motifsBMC Res. Notes.BMC Research Notes1157440CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8927http://bibliotecadigital.udea.edu.co/bitstream/10495/22179/2/license_rdf1646d1f6b96dbbbc38035efc9239ac9cMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/22179/3/license.txt8a4605be74aa9ea9d79846c1fba20a33MD53ORIGINALMosqueraJeanneth_EvolutionalBacterialAdoMet.pdfMosqueraJeanneth_EvolutionalBacterialAdoMet.pdfArtículo de investigaciónapplication/pdf2089635http://bibliotecadigital.udea.edu.co/bitstream/10495/22179/1/MosqueraJeanneth_EvolutionalBacterialAdoMet.pdf8448927ab06dc6a7d6c588174884557cMD5110495/22179oai:bibliotecadigital.udea.edu.co:10495/221792021-09-03 20:54:36.195Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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 |